The macromolecular crystallography beamline X06DA-PXIII has reached 1,000 structures in the Protein Data Bank (PDB) on February 22, 2017.
The macromolecular crystallography beamline X06DA-PXIII has reached 1,000 structures in the Protein Data Bank (PDB) on February 22, 2017. This performance has been achieved in only 9 years user operation and counts for about 2/3 of the available beamtime, which is proposed to academic users. The other 1/3 is used by researchers from international pharmaceutical companies in a partnership in place since the start of the beamline.
Looking at the number of PDB depositions, the super bending magnet (BM) beamline X06DA-PXIII is currently the best performing BM worldwide and is amongst the top 15 most productive beamlines, a ranking dominated by insertion device sources. X06DA-PXIII does exhibit performance comparable to undulators and therefore provides a very high throughput. In addition, X06DA-PXIII offers hardware [1] and software tools that are highly suited for experimental phasing [2], in particular native SAD (single-wavelength anomalous dispersion). The current increase in structures solved by native SAD reflects the routine use of a simple and fast data collection protocol developed at X06DA-PXIII [3,4].
An integrated crystallization facility further complements the beamline capabilities and contributes to help structural biologists getting crystallographic structures in the most efficient manner [5].
We warmly congratulate our long term users - A. Mitschler/A. Podjarny, A. Mattevi/S. Pasqualato, T. Maier and A. Prota/M. Steinmetz - who have deposited the 1,000th structure at X06DA-PXIII.
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Additional information
Biosync link to beamline statistics
Publications from the beamline
1. PRIGo: a new multi-axis goniometer for macromolecular crystallography
Waltersperger S., Olieric V., Pradervand C., Glettig W., Salathe M., Fuchs M.R., Curtin A., Wang X., Ebner S., Panepucci E., Weinert T., Schulze-Briese C., Wang M.
Journal of Synchrotron Radiation, 22(Pt 4):895-900, 2015
DOI: 10.1107/S1600577515005354
2. Advanced Crystallographic Data Collection Protocols for Experimental Phasing
Finke A.D., Panepucci E., Vonrhein C., Wang M., Bricogne G., Oliéric V.
Methods in Molecular Biology, 1320:175-91, 2016
DOI: 10.1007/978-1-4939-2763-0_11
3. Fast native SAD phasing for routine macromolecular structure determination
Weinert T., Olieric V., Waltersperger S., Panepucci E., Chen L., Zhang H., Zhou D., Rose J., Ebihara A., Kuramitsu S., Li D., Howe N., Schnapp G., Pautsch A., Bargsten K., Prota A., Surana P., Kottur J., Nair D., Basilico F., Cecatiello V., Pasqualato S., Boland A., Weichenrieder O., Wang B.C., Steinmetz M., Caffrey M., Wang M.
Nature Methods, 12(2):131-3, 2015
DOI: 10.1038/nmeth.3211
4. Data collection strategy for challenging native SAD phasing
Olieric V., Weinert T., Finke A.D., Anders C., Li D., Olieric N., Borca C, Steinmetz M.O., Caffrey M., Jinek M. and Wang M.
Acta Cryst. D72, 421-429, 2016
DOI: 10.1107/S2059798315024110
5. The SLS crystallization platform at beam-line X06DA - a fully automated pipeline enabling in situ X-ray diffraction screening.
Bingel-Erlenmeyer B., Olieric V., Grimshaw J.P.A., Gabadinho J., Wang X., Ebner S.G., Isenegger A., Schneider R., Schneider J., Glettig W., Pradervand C., Panepucci E.H., Tomizaki T., Wang M., Schulze-Briese C.
Crystal Growth & Design, 11 (4), pp 916–923, 2011
DOI: 10.1021/cg101375j